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Journal Abstract Search

169 related items for PubMed ID: 14581473

  • 1. Quantitative evaluation of the contribution of weak lysine-binding sites present within apolipoprotein(a) kringle IV types 6-8 to lipoprotein(a) assembly.
    Becker L, Cook PM, Wright TG, Koschinsky ML.
    J Biol Chem; 2004 Jan 23; 279(4):2679-88. PubMed ID: 14581473
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  • 3. Sequences within apolipoprotein(a) kringle IV types 6-8 bind directly to low-density lipoprotein and mediate noncovalent association of apolipoprotein(a) with apolipoprotein B-100.
    Gabel BR, Koschinsky ML.
    Biochemistry; 1998 May 26; 37(21):7892-8. PubMed ID: 9601051
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  • 4. Baboon lipoprotein(a) binds very weakly to lysine-agarose and fibrin despite the presence of a strong lysine-binding site in apolipoprotein(a) kringle IV type 10.
    Belczewski AR, Ho J, Taylor FB, Boffa MB, Jia Z, Koschinsky ML.
    Biochemistry; 2005 Jan 18; 44(2):555-64. PubMed ID: 15641780
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  • 9. Analysis of the mechanism of lipoprotein(a) assembly.
    Koschinsky ML, Marcovina SM, May LF, Gabel BR.
    Clin Genet; 1997 Nov 18; 52(5):338-46. PubMed ID: 9520124
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  • 10. Nuclear magnetic resonance (NMR) solution structure, dynamics, and binding properties of the kringle IV type 8 module of apolipoprotein(a).
    Chitayat S, Kanelis V, Koschinsky ML, Smith SP.
    Biochemistry; 2007 Feb 20; 46(7):1732-42. PubMed ID: 17263558
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  • 11. Apo(a) and ApoB Interact Noncovalently Within Hepatocytes: Implications for Regulation of Lp(a) Levels by Modulation of ApoB Secretion.
    Youssef A, Clark JR, Marcovina SM, Boffa MB, Koschinsky ML.
    Arterioscler Thromb Vasc Biol; 2022 Mar 20; 42(3):289-304. PubMed ID: 35045727
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  • 12. Identification of sequences in apolipoprotein(a) that maintain its closed conformation: a novel role for apo(a) isoform size in determining the efficiency of covalent Lp(a) formation.
    Becker L, Cook PM, Koschinsky ML.
    Biochemistry; 2004 Aug 10; 43(31):9978-88. PubMed ID: 15287725
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  • 13. Identification and analyses of inhibitors targeting apolipoprotein(a) kringle domains KIV-7, KIV-10, and KV provide insight into kringle domain function.
    Sandmark J, Tigerström A, Akerud T, Althage M, Antonsson T, Blaho S, Bodin C, Boström J, Chen Y, Dahlén A, Eriksson PO, Evertsson E, Fex T, Fjellström O, Gustafsson D, Herslöf M, Hicks R, Jarkvist E, Johansson C, Kalies I, Karlsson Svalstedt B, Kartberg F, Legnehed A, Martinsson S, Moberg A, Ridderström M, Rosengren B, Sabirsh A, Thelin A, Vinblad J, Wellner AU, Xu B, Östlund-Lindqvist AM, Knecht W.
    J Biol Chem; 2020 Apr 10; 295(15):5136-5151. PubMed ID: 32132173
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  • 17. Determinants of lipoprotein(a) assembly: a study of wild-type and mutant apolipoprotein(a) phenotypes isolated from human and rhesus monkey lipoprotein(a) under mild reductive conditions.
    Edelstein C, Mandala M, Pfaffinger D, Scanu AM.
    Biochemistry; 1995 Dec 19; 34(50):16483-92. PubMed ID: 8845377
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  • 18. Apo(a)-kringle IV-type 6: expression in Escherichia coli, purification and in vitro refolding.
    Hrzenjak A, Frank S, Maderegger B, Sterk H, Kostner GM.
    Protein Eng; 2000 Sep 19; 13(9):661-6. PubMed ID: 11054461
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  • 19. The apolipoprotein(a) component of lipoprotein(a) mediates binding to laminin: contribution to selective retention of lipoprotein(a) in atherosclerotic lesions.
    D'Angelo A, Geroldi D, Hancock MA, Valtulina V, Cornaglia AI, Spencer CA, Emanuele E, Calligaro A, Koschinsky ML, Speziale P, Visai L.
    Biochim Biophys Acta; 2005 Feb 21; 1687(1-3):1-10. PubMed ID: 15708348
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